1D4D: CRYSTAL STRUCTURE OF THE SUCCINATE COMPLEXED FORM OF THE FLAVOCYTOCHROME C FUMARATE REDUCTASE OF SHEWANELLA PUTREFACIENS STRAIN MR-1

Citation:
Abstract
Fumarate respiration is one of the most widespread types of anaerobic respiration. The soluble fumarate reductase of Shewanella putrefaciens MR-1 is a periplasmic tetraheme flavocytochrome c. The crystal structures of the enzyme were solved to 2.9 A for the uncomplexed form and to 2.8 A and 2.5 A for the fumarate and the succinate-bound protein, respectively. The structures reveal a flexible capping domain linked to the FAD-binding domain. A catalytic mechanism for fumarate reduction based on the structure of the complexed protein is proposed. The mechanism for the reverse reaction is a model for the homologous succinate dehydrogenase (complex II) of the respiratory chain. In flavocytochrome c fumarate reductase, all redox centers are in van der Waals contact with one another, thus providing an efficient conduit of electrons from the hemes via the FAD to fumarate.
PDB ID: 1D4DDownload
MMDB ID: 11454
PDB Deposition Date: 1999/10/3
Updated in MMDB: 1999/12
Experimental Method:
x-ray diffraction
Resolution: 2.5  Å
Source Organism:
Similar Structures:
Biological Unit for 1D4D: monomeric; determined by author
Molecular Components in 1D4D
Label Count Molecule
Protein (1 molecule)
1
Flavocytochrome C Fumarate Reductase(Gene symbol: fccA)
Molecule annotation
Chemicals (6 molecules)
1
4
2
1
3
1
* Click molecule labels to explore molecular sequence information.

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